The Role of the SRC Homology 2-Containing Inositol 5′-Phosphatase in FcɛR1-Induced Signaling
| Autor: | Cheryl D. Helgason, V. Duronio, R. K. Humphries, Jacqueline E. Damen, Gerald Krystal, Michael Huber, M. P. Scheid, Vivian Lam |
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| Rok vydání: | 1999 |
| Předmět: |
medicine.medical_specialty
B-cell receptor Signal transducing adaptor protein Tyrosine phosphorylation Biology Cell biology chemistry.chemical_compound Endocrinology chemistry Internal medicine Immunoreceptor tyrosine-based activation motif medicine Phosphorylation Tyrosine Signal transduction Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Current Topics in Microbiology and Immunology ISBN: 9783642636349 |
| DOI: | 10.1007/978-3-642-58537-1_3 |
| Popis: | In 1996, three groups independently cloned the hemopoietic specific src homology 2 (SH2)-containing inositol 5′-phosphatase, SHIP (Damen et al. 1996; Lioubin et al. 1996; Kavanaugh et al. 1996). Although this intracellular enzyme, which is capable in vitro of hydrolyzing the 5′-phosphate from phosphatidylinositol-3,4,5-trisphosphate (PIP3) and inositol-1,3,4,5-tetrakisphosphate (IP4) (Damen et al. 1996), was originally identified as a 145-kDa protein that became both tyrosine phosphorylated and associated with the adaptor protein Shc in response to multiple cytokines and to B- and T-cell receptor engagement (reviewed in Liu et al. 1997), it is currently in the limelight because of its interaction with the negative co-receptor FcγRIIB. Specifically, SHIP is now known to inhibit immune receptor-mediated activation in both mast cells and B cells by binding to the tyrosine phosphorylated immunoreceptor tyrosine-based inhibitory motif (ITIM) of the inhibitory core-ceptor FcγRIIB (Vely et al. 1997; Tridandapani et al. 1997) and inhibiting FcɛRl- and B cell receptor-induced degranulation and proliferation, respectively (Ono et al. 1996; Ono et al. 1997). However, while activation of the B cell receptor in the absence of FcγRIIB co-clustering does not lead to significant tyrosine phosphorylation of SHIP (Chacko et al. 1996), activation of the FcɛRl alone does (Huber et al. 1998). We therefore investigated whether SHIP plays any role in modulating IgE-induced signaling via this immunoreceptor tyrosine based activation motif (ITAM)-containing receptor in the absence of FcγRIIB co-clustering. In this review we discuss our findings in this area. |
| Databáze: | OpenAIRE |
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